- YUMAB® – Antibody discovery technologies
- The power of in-vitro antibody selection
- Challenging difficult targets by optimized discovery solutions
YUMAB® Antibody discovery technologies
YUMAB’s advanced in-vitro antibody generation pipeline employs phage display selection in combination with our proprietary universal naïve human antibody gene libraries or customized immune libraries.
The principle of antibody phage display is based on large libraries of bacteriophage particles, each carrying the genetic information and the unique phenotypic binding function of one antibody clone. In-vitro selection is performed by the molecular interaction of the target and the antibody phage. Several selection rounds result in the enrichment of antigen-specific antibody phage. Ultimately, monoclonal antibodies are identified by soluble expression and screening, using different types of immunoassays.
The power of in-vitro antibody selection
The selection is completely independent of animal immunizations and helps to reduce unnecessary animal experiments. Moreover, bypassing the in-vivo immune response has many advantages, particularly for difficult targets like highly conserved, non-immunogenic, instable, or toxic proteins.
YUMAB can tightly control biochemical conditions to guide antibody selection towards higher specificity and lower cross-reactivity, respectively. Specificity and cross-reactivity can even be targeted to certain epitopes, e.g. shared epitopes of the human and murine protein. We can also match your final assay conditions (e.g., buffer, salt, pH, allosteric conformation of the antigen, competitors, etc.) during in-vitro selection to generate antibodies that will work better for your application.
Challenging difficult targets by optimized discovery solutions
Today, most antibody discovery campaigns aim to target ‘difficult’ multi-pass-transmembrane proteins like GPCRs or ion channels. Since the production of soluble recombinant antigens remain challenging in these cases, YUMAB developed an optimized discovery solution that directly uses antigen-positive cells as a target antigen during the antibody selection.
The cells can either be transfected transiently with the transgene of interest, or stable, antigen-overexpressing cell lines can be used.
Since the antibody selection is done on the cellular protein instead of a recombinant protein, the binding epitope of the identified antibodies is restricted to native, functional and accessible epitopes on the cell surface. Consequently, a higher rate of biologic active antibodies can be found in the output. Additionally, antibodies identified by cell selection usually show a higher selectivity and specificity, since binding to other surface proteins is strictly controlled and prevented.
Science Campus Braunschweig-Süd
38124 Braunschweig – Germany
Phone: +49 531 481170-0